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Titolo:
CD6 RECOGNIZES THE NEURAL ADHESION MOLECULE BEN
Autore:
SKONIER JE; BOWEN MA; ARUFFO A; BAJORATH J;
Indirizzi:
BRISTOL MYERS SQUIBB PHARMACEUT RES INST,3005 1SST AVE SEATTLE WA 98121 BRISTOL MYERS SQUIBB PHARMACEUT RES INST SEATTLE WA 98121 UNIV WASHINGTON,DEPT BIOL STRUCT SEATTLE WA 98195
Titolo Testata:
Protein science
fascicolo: 8, volume: 6, anno: 1997,
pagine: 1768 - 1770
SICI:
0961-8368(1997)6:8<1768:CRTNAM>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNOGLOBULIN SUPERFAMILY; CELL-SURFACE; DOMAIN; LIGAND; CONTAINS; ANTIGEN; FAMILY; ALCAM;
Keywords:
BINDING AVIDITY; CD166; CD6; CELL SURFACE RECEPTOR-LIGAND INTERACTION; RESIDUE CONSERVATION; SPECIFICITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
15
Recensione:
Indirizzi per estratti:
Citazione:
J.E. Skonier et al., "CD6 RECOGNIZES THE NEURAL ADHESION MOLECULE BEN", Protein science, 6(8), 1997, pp. 1768-1770

Abstract

CD6 and its ligand activated leukocyte cell adhesion molecule (ALCAM,CD166) have been detected on various immune cells and in the brain. CD6-ligand interactions have been implicated in the regulation of T cell function. ALCAM shares the same extracellular domain organization and significant sequence homology with the chicken neural adhesion molecule BEN. Although ALCAM's CD6 binding site is only partially conservedin BEN, CD6 specifically binds BEN, albeit with similar to 10-fold lower avidity than ALCAM. Differences in binding avidity are not detected when ALCAM and BEN fusion proteins containing the full-length extracellular regions are tested. Homotypic interactions between full-lengthforms are likely to account for these observations. The identified cross-species interaction between CD6 and BEN suggests that CD6-ligand interactions are highly conserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 09:04:18